{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["107(4)"],"submitter":["Hilsch M"],"pubmed_abstract":["The matrix protein M1 plays a pivotal role in the budding of influenza virus from the plasma membrane (PM) of infected cells. This protein interacts with viral genetic material and envelope proteins while binding to the inner leaflet of the PM. Its oligomerization is therefore closely connected to the assembly of viral components and the formation of new virions. Of interest, the molecular details of M1 interaction with lipids and other viral proteins are far from being understood, and it remains to be determined whether the multimerization of M1 is affected by its binding to the PM and interaction with its components. To clarify the connection between M1 oligomerization and binding to lipid membranes, we applied a combination of several quantitative microscopy approaches. First, we used n"],"journal":["Biophysical journal"],"pagination":["912-23"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4142230"],"repository":["biostudies-literature"],"pubmed_title":["Influenza A matrix protein M1 multimerizes upon binding to lipid membranes."],"pmcid":["PMC4142230"],"pubmed_authors":["Sieben C","Klipp E","Chiantia S","Hilsch M","Rabe JP","Herrmann A","Goldenbogen B","Hofer CT"],"additional_accession":[]},"is_claimable":false,"name":"Influenza A matrix protein M1 multimerizes upon binding to lipid membranes.","description":"The matrix protein M1 plays a pivotal role in the budding of influenza virus from the plasma membrane (PM) of infected cells. This protein interacts with viral genetic material and envelope proteins while binding to the inner leaflet of the PM. Its oligomerization is therefore closely connected to the assembly of viral components and the formation of new virions. Of interest, the molecular details of M1 interaction with lipids and other viral proteins are far from being understood, and it remains to be determined whether the multimerization of M1 is affected by its binding to the PM and interaction with its components. To clarify the connection between M1 oligomerization and binding to lipid membranes, we applied a combination of several quantitative microscopy approaches. First, we used n","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Aug","modification":"2025-04-26T09:08:22.098Z","creation":"2019-03-27T01:34:34Z"},"accession":"S-EPMC4142230","cross_references":{"pubmed":["25140426"],"doi":["10.1016/j.bpj.2014.06.042"]}}